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Bioorg Med Chem Lett. 2010 Apr 1;20(7):2103-5. doi: 10.1016/j.bmcl.2010.02.069. Epub 2010 Feb 20.

Toward the development of potent and selective bisubstrate inhibitors of protein arginine methyltransferases.

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  • 1School of Chemistry, University Park, University of Nottingham, Nottingham, NG7 2RD, UK.


Prototype inhibitors of protein arginine methyltransferases (PRMTs) have been constructed by attaching guanidine functionality via a variable linker to non-reactive amine analogues of the cellular co-factor (S)-adenosyl methionine (AdoMet). Potent inhibition of PRMT1 (IC(50) of approximately 3-6 microM) combined with weak inhibition of the lysine methyltransferase SET7 (approximately 50% of activity at 100 microM) was observed for two such compounds.

2010 Elsevier Ltd. All rights reserved.

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